5EZ3
Crystal structure Acyl-CoA dehydrogenase from Brucella melitensis in complex with FAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue FAD A 600 |
| Chain | Residue |
| A | MET190 |
| A | TRP433 |
| A | GLU434 |
| A | SER436 |
| A | ASN438 |
| A | LEU442 |
| A | HOH740 |
| A | HOH747 |
| A | HOH751 |
| A | HOH777 |
| A | HOH807 |
| A | MET192 |
| A | HOH848 |
| A | HOH927 |
| B | ARG332 |
| B | VAL334 |
| B | PHE335 |
| B | LEU339 |
| B | GLN342 |
| B | MET345 |
| B | GLU407 |
| B | CYS408 |
| A | THR193 |
| B | GLY410 |
| B | GLY411 |
| A | GLY197 |
| A | GLY198 |
| A | THR199 |
| A | PHE224 |
| A | SER226 |
| A | VAL429 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MRD A 601 |
| Chain | Residue |
| A | LEU141 |
| A | CYS142 |
| A | THR145 |
| A | ASP309 |
| A | ALA313 |
| A | ASN430 |
| A | TRP433 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue MPD A 602 |
| Chain | Residue |
| A | ASP301 |
| A | PHE370 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CAC A 603 |
| Chain | Residue |
| A | LEU548 |
| A | HOH769 |
| A | HOH996 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | binding site for residue FAD B 600 |
| Chain | Residue |
| A | ARG332 |
| A | VAL334 |
| A | PHE335 |
| A | LEU339 |
| A | GLN342 |
| A | MET345 |
| A | GLU407 |
| A | CYS408 |
| A | GLY410 |
| A | GLY411 |
| B | MET190 |
| B | MET192 |
| B | THR193 |
| B | GLY197 |
| B | GLY198 |
| B | THR199 |
| B | PHE224 |
| B | SER226 |
| B | VAL429 |
| B | TRP433 |
| B | GLU434 |
| B | SER436 |
| B | ASN438 |
| B | LEU442 |
| B | HOH720 |
| B | HOH724 |
| B | HOH777 |
| B | HOH782 |
| B | HOH841 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue MRD B 601 |
| Chain | Residue |
| B | LEU141 |
| B | CYS142 |
| B | THR145 |
| B | ASP309 |
| B | ALA313 |
| B | ASN430 |
| B | TRP433 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CAC B 603 |
| Chain | Residue |
| B | PRO33 |
| B | GLY511 |
| B | ALA512 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CAC B 604 |
| Chain | Residue |
| B | GLN163 |
| B | TRP164 |
| B | ALA180 |
| B | PHE181 |
| site_id | AC9 |
| Number of Residues | 29 |
| Details | binding site for residue FAD C 600 |
| Chain | Residue |
| C | LEU442 |
| C | HOH765 |
| C | HOH776 |
| C | HOH795 |
| C | HOH797 |
| C | HOH812 |
| C | HOH825 |
| D | ARG332 |
| D | VAL334 |
| D | LEU339 |
| D | GLN342 |
| D | MET345 |
| D | GLU407 |
| D | CYS408 |
| D | GLY410 |
| D | GLY411 |
| C | MET190 |
| C | MET192 |
| C | THR193 |
| C | GLY197 |
| C | GLY198 |
| C | THR199 |
| C | PHE224 |
| C | SER226 |
| C | VAL429 |
| C | TRP433 |
| C | GLU434 |
| C | SER436 |
| C | ASN438 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue MRD C 601 |
| Chain | Residue |
| C | LEU141 |
| C | CYS142 |
| C | THR145 |
| C | ASP309 |
| C | CYS310 |
| C | ALA313 |
| C | ASN430 |
| C | TRP433 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue CAC C 603 |
| Chain | Residue |
| C | PRO33 |
| C | LEU34 |
| C | GLY511 |
| C | ALA512 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CAC C 604 |
| Chain | Residue |
| C | GLN163 |
| C | TRP164 |
| C | ALA180 |
| C | PHE181 |
| site_id | AD4 |
| Number of Residues | 30 |
| Details | binding site for residue FAD D 600 |
| Chain | Residue |
| C | ARG332 |
| C | VAL334 |
| C | PHE335 |
| C | LEU339 |
| C | GLN342 |
| C | MET345 |
| C | GLU407 |
| C | CYS408 |
| C | GLY410 |
| C | GLY411 |
| D | MET190 |
| D | MET192 |
| D | THR193 |
| D | GLY197 |
| D | GLY198 |
| D | THR199 |
| D | PHE224 |
| D | SER226 |
| D | VAL429 |
| D | TRP433 |
| D | GLU434 |
| D | SER436 |
| D | ASN438 |
| D | VAL439 |
| D | LEU442 |
| D | HOH724 |
| D | HOH730 |
| D | HOH776 |
| D | HOH777 |
| D | HOH843 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue MRD D 601 |
| Chain | Residue |
| D | PHE130 |
| D | LEU141 |
| D | CYS142 |
| D | THR145 |
| D | ASP309 |
| D | ASN430 |
| D | TRP433 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue CAC D 604 |
| Chain | Residue |
| D | GLN163 |
| D | TRP164 |
| D | PHE181 |
| D | HOH785 |
Functional Information from PROSITE/UniProt
